GIPC, a PDZ domain containing protein, interacts specifically with the C terminus of RGS-GAIP
about
MIR16, a putative membrane glycerophosphodiester phosphodiesterase, interacts with RGS16PDZ domain protein GIPC interacts with the cytoplasmic tail of melanosomal membrane protein gp75 (tyrosinase-related protein-1)CD93 interacts with the PDZ domain-containing adaptor protein GIPC: implications in the modulation of phagocytosisMyo6 facilitates the translocation of endocytic vesicles from cell peripheriesThe neuropilin 1 cytoplasmic domain is required for VEGF-A-dependent arteriogenesisRGS3 interacts with 14-3-3 via the N-terminal region distinct from the RGS (regulator of G-protein signalling) domainGipc3 mutations associated with audiogenic seizures and sensorineural hearing loss in mouse and human.GIPC and GAIP form a complex with TrkA: a putative link between G protein and receptor tyrosine kinase pathwaysClathrin-coated vesicles bearing GAIP possess GTPase-activating protein activity in vitroPromotion of G alpha i3 subunit down-regulation by GIPN, a putative E3 ubiquitin ligase that interacts with RGS-GAIPMembrane-associated GAIP is a phosphoprotein and can be phosphorylated by clathrin-coated vesiclesRole of PDZ proteins in regulating trafficking, signaling, and function of GPCRs: means, motif, and opportunityStructural Insights into the Inhibition of Wnt Signaling by Cancer Antigen 5T4/Wnt-Activated Inhibitory Factor 1Erk1/2-dependent phosphorylation of Galpha-interacting protein stimulates its GTPase accelerating activity and autophagy in human colon cancer cellsSema4c, a transmembrane semaphorin, interacts with a post-synaptic density protein, PSD-95Synectin, syndecan-4 cytoplasmic domain binding PDZ protein, inhibits cell migrationA PDZ protein regulates the distribution of the transmembrane semaphorin, M-SemFGIPC interacts with the beta1-adrenergic receptor and regulates beta1-adrenergic receptor-mediated ERK activationGIPC binds to the human lutropin receptor (hLHR) through an unusual PDZ domain binding motif, and it regulates the sorting of the internalized human choriogonadotropin and the density of cell surface hLHRA PDZ domain protein interacts with the C-terminal tail of the insulin-like growth factor-1 receptor but not with the insulin receptorPDZ interaction sites in integrin alpha subunits. T14853, TIP/GIPC binds to a type I recognition sequence in alpha 6A/alpha 5 and a novel sequence in alpha 6BBDNF-mediated neurotransmission relies upon a myosin VI motor complexGLUT1CBP(TIP2/GIPC1) interactions with GLUT1 and myosin VI: evidence supporting an adapter function for GLUT1CBPBinding of internalized receptors to the PDZ domain of GIPC/synectin recruits myosin VI to endocytic vesiclesGAIP interacting protein C-terminus regulates autophagy and exosome biogenesis of pancreatic cancer through metabolic pathwaysInteractions of GIPC with dopamine D2, D3 but not D4 receptors define a novel mode of regulation of G protein-coupled receptorsExpression of myosin VI within the early endocytic pathway in adult and developing proximal tubulesThe cytoplasmic domain of neuropilin 1 is dispensable for angiogenesis, but promotes the spatial separation of retinal arteries and veinsMolecular basis of semaphorin-mediated axon guidanceRegulators of G Protein SignalingG protein selectivity is a determinant of RGS2 function.Neuropilin-1 stimulates tumor growth by increasing fibronectin fibril assembly in the tumor microenvironmentFunctional proteomics, human genetics and cancer biology of GIPC family membersMyosin VI is required for targeted membrane transport during cytokinesis.Uncoated endocytic vesicles require the unconventional myosin, Myo6, for rapid transport through actin barriers.Synectin in the nervous system: expression pattern and potential as a binding partner of neurotrophin receptors.Human papillomavirus type 18 E6 protein binds the cellular PDZ protein TIP-2/GIPC, which is involved in transforming growth factor beta signaling and triggers its degradation by the proteasomeA human monoclonal autoantibody to breast cancer identifies the PDZ domain containing protein GIPC1 as a novel breast cancer-associated antigen.VEGF targets the tumour cell.The Drosophila GIPC homologue can modulate myosin based processes and planar cell polarity but is not essential for development.
P2860
Q22253864-656DF1CD-FC79-4CE5-9A27-9132E4271D8BQ24291415-720FC6A7-3D85-4AAD-97CA-0246D3CAFF98Q24305979-AFE9FFA1-357F-4CD5-8154-F67371F16CEBQ24307920-76454AF6-65F3-4212-8DA5-6ECF972BDA9BQ24339531-61DC5CC1-F6F6-42AC-A735-CE22837C76AAQ24534291-0D99E523-244D-4AF3-AEEA-5339284CEA32Q24629226-7319E6CA-12CC-484D-BA48-C647251A3ACCQ24633321-B348F546-C98D-49E7-8D0C-8196BC9BC6E9Q24653707-4507BBBC-0447-47B8-B336-DD644682AC2EQ24680028-E04BE3B4-8953-468E-B6C8-20FC5352BA33Q24682851-DADC08E2-5563-4912-A4FA-26FA5E9B0DB6Q27015870-603A70EB-1F7C-478D-975C-B7597DE00306Q27681929-FD5BEA70-FD7E-4B05-AF34-46409A50B33BQ28138966-5209E271-5D29-4E76-854D-2CE32493610CQ28141233-B4F7471B-DE00-496A-9333-09C4AC975B21Q28141795-FDC3E112-41B3-47A1-A550-B0CFED7C0BCDQ28143494-50225945-4431-41F3-B04B-18CB14B7EFB0Q28201893-6A1FD361-3520-4BC1-848A-52306268DADBQ28204866-A55E3DF7-9934-4F9E-AAC7-307C14106605Q28205584-21FA697E-6044-45C6-90C6-56C6240ADE79Q28209987-6A75DF8B-34DA-45E5-8074-3F9EAC2CC28CQ28510749-3F535693-EC1D-4B13-8202-78B00DF35CC2Q28511940-042E1666-7438-459A-A0C0-88CFCE3FBC50Q28511953-99B1FEFB-EB1D-493D-BA9E-56FC54F05CD8Q28542464-40E34DB7-589A-411C-833E-0432516FDCDFQ28573869-F4497F38-0FF0-468D-AC43-933F351DC73FQ28579268-C34AE2A3-5334-4020-AE62-8F85E6EABBBBQ28590445-FC8BF3F1-879A-45FE-ADC7-94162343337CQ28611466-97E2313F-9016-4C06-AEC4-33511787F07FQ29302980-16EF8F3B-672B-4DF0-8AE7-350132CB9C10Q30323308-BACA5DDB-CE86-45F3-93E0-DEBC8A18D204Q30450729-59384130-13E4-430F-85E9-CB6C1E1D7D0BQ30452637-765AB225-19C0-4FDB-B9F6-D7BF9E815C45Q30480755-9557F896-DFFC-4BDA-84BA-49109C3F21C0Q30579400-EA57E834-7F54-44C6-9ECC-CA6FC333B74BQ33288797-8FFEA70D-5D7C-4170-841E-581A072BAFEAQ33292234-472B9149-FD41-45EC-AA84-5B904DD484DFQ33362597-6F1F6768-CCCB-4388-BED0-FBCBB8FA674DQ33573324-170ECFB1-174C-47D0-9334-A0D57A916650Q33614673-05532B8A-ECC9-4C2E-AE17-6FB8ACAC10CE
P2860
GIPC, a PDZ domain containing protein, interacts specifically with the C terminus of RGS-GAIP
description
1998 nî lūn-bûn
@nan
1998 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
GIPC, a PDZ domain containing ...... ith the C terminus of RGS-GAIP
@ast
GIPC, a PDZ domain containing ...... ith the C terminus of RGS-GAIP
@en
GIPC, a PDZ domain containing ...... ith the C terminus of RGS-GAIP
@en-gb
GIPC, a PDZ domain containing ...... ith the C terminus of RGS-GAIP
@nl
type
label
GIPC, a PDZ domain containing ...... ith the C terminus of RGS-GAIP
@ast
GIPC, a PDZ domain containing ...... ith the C terminus of RGS-GAIP
@en
GIPC, a PDZ domain containing ...... ith the C terminus of RGS-GAIP
@en-gb
GIPC, a PDZ domain containing ...... ith the C terminus of RGS-GAIP
@nl
prefLabel
GIPC, a PDZ domain containing ...... ith the C terminus of RGS-GAIP
@ast
GIPC, a PDZ domain containing ...... ith the C terminus of RGS-GAIP
@en
GIPC, a PDZ domain containing ...... ith the C terminus of RGS-GAIP
@en-gb
GIPC, a PDZ domain containing ...... ith the C terminus of RGS-GAIP
@nl
P2093
P2860
P356
P1476
GIPC, a PDZ domain containing ...... ith the C terminus of RGS-GAIP
@en
P2093
P2860
P304
P356
10.1073/PNAS.95.21.12340
P407
P577
1998-10-13T00:00:00Z